A Deubiquitinating Activity Is Conserved in the Large Tegument Protein of the Herpesviridae.

by: Christian Schlieker, Gregory A A Korbel, Lisa M M Kattenhorn, Hidde L L Ploegh

J Virol, Vol. 79, No. 24. (December 2005), pp. 15582-15585.

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Abstract

The largest tegument protein of herpes simplex virus 1 (HSV-1), UL36, contains a novel deubiquitinating activity embedded in it. All members of the Herpesviridae contain a homologue of HSV-1 UL36, the N-terminal segments of which show perfect conservation of those residues implicated in catalysis. For murine cytomegalovirus and Epstein-Barr virus, chosen as representatives of the beta- and gammaherpesvirus subfamilies, respectively, we here show that the homologous modules indeed display deubiquitinating activity in vitro. The conservation of this activity throughout all subfamilies is indicative of an important, if not essential, function.

@article{citeulike:408442, abstract = {The largest tegument protein of herpes simplex virus 1 (HSV-1), UL36, contains a novel deubiquitinating activity embedded in it. All members of the Herpesviridae contain a homologue of HSV-1 UL36, the N-terminal segments of which show perfect conservation of those residues implicated in catalysis. For murine cytomegalovirus and Epstein-Barr virus, chosen as representatives of the beta- and gammaherpesvirus subfamilies, respectively, we here show that the homologous modules indeed display deubiquitinating activity in vitro. The conservation of this activity throughout all subfamilies is indicative of an important, if not essential, function.}, address = {Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, 9 Cambridge Center, Cambridge, MA 02142. ploegh@wi.mit.edu.}, author = {Schlieker, Christian and Korbel, Gregory A A. and Kattenhorn, Lisa M M. and Ploegh, Hidde L L. }, citeulike-article-id = {408442}, doi = {http://dx.doi.org/10.1128/JVI.79.24.15582-15585.2005}, issn = {0022-538X}, journal = {J Virol}, keywords = {herpes, ubiquitin}, month = {December}, number = {24}, pages = {15582--15585}, posted-at = {2005-12-12 20:18:23}, priority = {2}, title = {A Deubiquitinating Activity Is Conserved in the Large Tegument Protein of the Herpesviridae.}, url = {http://dx.doi.org/10.1128/JVI.79.24.15582-15585.2005}, volume = {79}, year = {2005} }

RIS record

TY - JOUR ID - citeulike:408442 L3 - citeulike-article-id:408442 TI - A Deubiquitinating Activity Is Conserved in the Large Tegument Protein of the Herpesviridae. JF - J Virol VL - 79 IS - 24 SP - 15582 EP - 15585 AD - Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, 9 Cambridge Center, Cambridge, MA 02142. ploegh@wi.mit.edu. SN - 0022-538X N2 - The largest tegument protein of herpes simplex virus 1 (HSV-1), UL36, contains a novel deubiquitinating activity embedded in it. All members of the Herpesviridae contain a homologue of HSV-1 UL36, the N-terminal segments of which show perfect conservation of those residues implicated in catalysis. For murine cytomegalovirus and Epstein-Barr virus, chosen as representatives of the beta- and gammaherpesvirus subfamilies, respectively, we here show that the homologous modules indeed display deubiquitinating activity in vitro. The conservation of this activity throughout all subfamilies is indicative of an important, if not essential, function. KW - herpes KW - ubiquitin AU - Schlieker, Christian AU - Korbel, Gregory A AU - Kattenhorn, Lisa M AU - Ploegh, Hidde L PY - 2005/12// UR - http://dx.doi.org/10.1128/JVI.79.24.15582-15585.2005 ER -

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